title: Human recombinant interleukin-1 alpha increases elastase-like enzyme in human uterine cervical fibroblasts.
abstract: Production of the elastase-like enzyme, Suc-(Ala)3-p-nitroanilide hydrolase, was examined in human uterine cervical fibroblasts. The metallo-dependent enzyme is present in both media and cellular fractions. Human recombinant interleukin-1 alpha stimulated cells to produce and secrete this elastase-like enzyme. These results suggest that modulation of this enzyme activity by interleukin-1 may play a significant role in the ripening and dilation of the cervix, because elastin is a component of the uterine cervix and its peptides are known to be chemotactic for leukocytes.
authors.affiliation: Department of Biochemistry, Tokyo College of Pharmacy, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Ito
authors.forename: P C
authors.initials: PC
authors.lastname: Leppert
authors.forename: Y
authors.initials: Y
authors.lastname: Mori
mesh_terms: D002478:Cells, Cultured; D002584:Cervix Uteri / Q000201:enzymology*; D005260:Female; D005347:Fibroblasts; D006801:Humans; D066298:In Vitro Techniques; D007375:Interleukin-1 / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000494:pharmacology
chemical_list: D007375:Interleukin-1; D011994:Recombinant Proteins; D010447:Peptide Hydrolases; C023092:succinyltrialanine p-nitroanilide hydrolase